id stringlengths 14 14 | text stringlengths 9 3.55k | source stringlengths 1 250 |
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c_sqjozuclslrp | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U43 is encoded in intron 1 of the ribosomal protein L3 gene in human and cow. Three other snoRNAs ( U82, U83a and U83b) are also encoded in the same host gene but from different introns. The Arabidopsis thaliana homologue is called snoR41 in the public sequence databases (Genbank). The rice homologue is expressed from a cluster also containing snoR16.U43 is hypothesised to guide methylation of 2'-O-ribose residues on 18S ribosomal RNA. | Small nucleolar RNA SNORD43 |
c_nibelggx0kuj | In molecular biology, snoRNA U44 (also known as SNORD44) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U44 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | Small nucleolar RNA SNORD44 |
c_mlxbcasp1flr | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U44 was originally cloned from HeLa cells and expression verified by northern blotting. It is predicted to guide 2'O-ribose methylation of 18S ribosomal RNA(rRNA) at residue A166. In the human genome, U44 is located in the same gene as several other C/D box snoRNAs (U47, U74, U75, U76, U77, U78, U79, U80 and U81). | Small nucleolar RNA SNORD44 |
c_0ugdku88htxi | In molecular biology, snoRNA U45 (also known as SNORD45) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA SNORD45 |
c_6exak97d8ikd | snoRNA U45 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U45 was originally cloned from HeLa cells and expression verified by northern blotting. It is related to the snoRNA (MBII-401) identified in mouseIn the human genome there are three very closely related copies of snoRNA U45 (called U45A, U45B, U45C) located within the introns of the same host gene. | Small nucleolar RNA SNORD45 |
c_kc7p2cm14rq3 | In molecular biology, snoRNA U46 (also known as SNORD46) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U46 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | Small nucleolar RNA SNORD46 |
c_lth1lxhvaudk | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U46 is encoded in intron 2 of the ribosomal protein S8 gene in human, and is hypothesised to guide methylation of 2'-O-ribose residues on 28S ribosomal RNA (rRNA). The homologue of this snoRNA in Arabidopsis thaliana is called snoZ153. Some human U40 sequences have been annotated in the sequence databases (Genbank) as U46. | Small nucleolar RNA SNORD46 |
c_et9fkortbmuo | In molecular biology, snoRNA U49 (also known as SNORD49) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA SNORD49 |
c_ssrynpeopzws | snoRNA U49 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U49 was identified by cloning from HeLa cells and is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) residue C4426. In the human genome there are two related copies of U45 (called U45A and U45B) which are encoded in the introns of the same host gene (MGC40157). | Small nucleolar RNA SNORD49 |
c_sbcctqdgtij7 | In molecular biology, snoRNA U50 (also known as SNORD50) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U50 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | Small nucleolar RNA SNORD50 |
c_u2z63qbdzg8r | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U50 is an intronic snoRNA gene located on chromosome 6q15, at the breakpoint of chromosomal translocation t(3;6)(q27;q15). The U50HG gene is composed of six exons, whose spliced transcripts have little potential for coding a protein, and its introns produce both U50 and U50-like (U50') snoRNAs that are localised in nucleoli. There is evidence that the U50 paralogues form a novel family of genes controlling oncogenesis and sensitivity to therapy in cancer. | Small nucleolar RNA SNORD50 |
c_z7n8ms4zpnnq | In molecular biology, snoRNA U52 (also known as SNORD52) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U52 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U52 was originally cloned from HeLa cells and is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) residue U3904. U52 and the C/D box snoRNA U48 are encoded in the introns of the same host gene (C6orf48). | Small nucleolar RNA SNORD52 |
c_o0p8dj4ut2uj | In molecular biology, snoRNA U53 (also known as SNORD53) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA SNORD53 |
c_lbyowmr29vdy | snoRNA U53 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U53 was originally cloned from HeLa cells and is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) at residue C3848. It is related to mouse snoRNA MBII-35 | Small nucleolar RNA SNORD53 |
c_a5fn3ofxh5qx | In molecular biology, snoRNA U56 (also known as SNORD56) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U56 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | Small nucleolar RNA SNORD56 |
c_al10lbijbv5i | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U56 was originally cloned from HeLa cells and is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue C517. In the human genome U56 is encoded in the introns of the same host gene as several other snoRNAs (C/D box snoRNAs U57, U86 and HBII-55, and the H/ACA box snoRNA ACA51). This host gene encodes Nucleolar Protein 5A (NOL5A). | Small nucleolar RNA SNORD56 |
c_bfogkhcppjiu | In molecular biology, snoRNA U57 (also known as SNORD57) is a member of the C/D box class of snoRNAs. This family functions to direct site-specific 2'-O-methylation of substrate RNAs.This snoRNA was originally cloned from human HeLa cells during a screen for intron encoded snoRNAs. It is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) at residue A99 3 | Small nucleolar RNA SNORD57 |
c_fvs4wgaei72h | In molecular biology, snoRNA U58 (also known as SNORD58) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U57 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | Small nucleolar RNA SNORD58 |
c_a5pyp6vnia8f | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.In the human genome there are two closely related copies of U85 (called U58A and U58B). They are both encoded in the introns of the ribosomal protein RPL17 gene. Both snoRNAs are predicted to guide 2'O-ribose methylation of the large 28S ribosomal RNA (rRNA) subunit on residue G4198. | Small nucleolar RNA SNORD58 |
c_qxj65sglrmjx | In molecular biology, snoRNA U59 is an RNA molecule that belongs to the C/D class of snoRNA, which contain the C box motif (UGAUGA) and the D box motif (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. There are two closely related copies of U59, called SNORD59A and SNORD59B. They are both expressed from the intron of the host gene ATP5A. | Small nucleolar RNA SNORD59 |
c_yd3qjszitxrb | Both SNORD59A and SNORD59B target the 2'-O-methylation of 18S rRNA position A1031. This RNA has been identified in both the human and mouse genomes. Not to be confused with the plant snoRNA U59. | Small nucleolar RNA SNORD59 |
c_114sf11ee993 | In molecular biology, snoRNA U61 (also known as SNORD61) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U61 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U61 snoRNA was cloned from HeLa cells and is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue U1442. | Small nucleolar RNA SNORD61 |
c_lw6dmcprygct | In molecular biology, snoRNA U62 (also known as SNORD62) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA SNORD62 |
c_90v5wkh94wcm | snoRNA U62 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.In the human genome there are two identical copies of snoRNA U62 (called U62A and U62B) both of which are located within the introns of the same host gene which encodes a hypothetical protein (KIAA0515). U62 is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue A590. | Small nucleolar RNA SNORD62 |
c_6gx6ztvxgzut | In molecular biology, snoRNA U63 (also known as SNORD63) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA SNORD63 |
c_0dg3u53ltgfo | snoRNA U63 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.snoRNA U63 was purified from HeLa cells by immunoprecipitation with antifibrillarin antibody. It is predicted to guide the 2'-O-ribose methylation of 28s ribosomal RNA (rRNA) at residue A4531. | Small nucleolar RNA SNORD63 |
c_6vkfzy1bym6v | In molecular biology, snoRNA U67 is a non-coding RNA molecule that belongs to the H/ACA class of snoRNAs which are thought to guide the sites of modification of uridines to pseudouridines. This snoRNA guides pseudouridylation of position U1445 in 18S rRNA. This RNA is expressed from the intron of the host gene EIF4A1. | Small nucleolar RNA SNORA67 |
c_e1t5ecgn5u1n | In molecular biology, snoRNA U79 (also known as SNORD79 or Z22) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA SNORD79 |
c_ojy3kxvgdk8s | U79 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.snoRNA U79 is found in intron 7 of the GAS5 gene in humans and is also present in mice. U79 is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) residue A3809. | Small nucleolar RNA SNORD79 |
c_mn0uwr05r2qo | In molecular biology, snoRNA U82 (also known as SNORD82 or Z25) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA U82/Z25 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | Small nucleolar RNA SNORD82 |
c_sef5ixsnkro1 | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.snoRNA U82 has been identified in both humans and mice: it is located in the fifth intron of the nucleolin gene in both species. Two additional snoRNAs (C/D box snoRNA U20 and the H/ACA snoRNA U23 ) are also encoded within the introns of the nucleolin gene.U82 is predicted to guide the 2'O-ribose methylation of 18S ribosomal RNA (rRNA) residue A1678.Another, different snoRNA, named U82 has been predicted in the introns of L3 ribosomal protein gene (RPL3) in humans and cows. However, the expression of this snoRNA could not be confirmed by northern blotting or Reverse transcription polymerase chain reaction (RT-PCR) and it should not be confused with this snoRNA located in the nucleolin gene. | Small nucleolar RNA SNORD82 |
c_ri89tlwi54sq | In molecular biology, snoRNA U95 (also known as SNORD95 or Z38) is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA SNORD95 |
c_b8txp5jgu3m4 | snoRNA U95 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.U95 was identified by computational screening of the introns of ribosomal protein genes for conserved C/D box sequence motifs and expression experimentally verified by northern blotting. U95 is predicted to guide the 2'O-ribose methylation of 28S ribosomal RNA (rRNA) residues A2802 and C2811. | Small nucleolar RNA SNORD95 |
c_dkms1c38wxz2 | In molecular biology, snoRNA Z17 is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. snoRNA Z17 is a member of the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). | Small nucleolar RNA Z17 |
c_8jhkyt814vf0 | Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. snoRNA Z17B is predicted to guide the 2'-O-ribose methylation of 18S rRNA at position U121. Two forms of this snoRNA are found in the intron of the ribosomal protein L23a gene. | Small nucleolar RNA Z17 |
c_cirsakgrlpvs | In molecular biology, snoRNA Z199 is a non-coding RNA (ncRNA) molecule which functions in the biogenesis (modification) of other small nuclear RNAs (snRNAs). This type of modifying RNA is located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA Z199 |
c_yudjdkfao9tm | snoRNA Z199 is a member of the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs.snoZ199 is predicted to be a methylation guide for sites on 18S and 25S ribosomal RNA (rRNA). Oryza sativa snoZ199 is reported to be homologous to Arabidopsis thaliana snoR13. | Small nucleolar RNA Z199 |
c_1qv5sqj0txot | In molecular biology, snoRNA Z37 is a member of the C/D class of snoRNA which contain the C (UGAUGA) and D (CUGA) box motifs. Z37 acts as a methylation guide for 5.8S ribosomal RNA. This family contains a putative snoRNA found in the intron of the receptor for activated C kinase (RACK1) gene in mammals identified by the Rfam database. This family also includes human snoRNAs U96a and U96b and the apicomplexan snoRNA snr39b. | Small nucleolar RNA Z37 |
c_gdhlrf5yyfrq | In molecular biology, snoRNA snR57 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA snR57 |
c_p3sn0ywvdpzc | snoRNA snR57 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. snoRNA snR57 was initially discovered using a computational screen of the Saccharomyces cerevisiae genome. | Small nucleolar RNA snR57 |
c_fs0kj6pv9hxj | In molecular biology, snoRNA snR69 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA snR69 |
c_3wn981z4rvbu | snoRNA snR69 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. snoRNA snR69 was initially discovered using a computational screen of the Saccharomyces cerevisiae genome. | Small nucleolar RNA snR69 |
c_6i55bqre6y1q | In molecular biology, snoRNA snR71 is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA. | Small nucleolar RNA snR71 |
c_2t69eob9cxk7 | snoRNA snR71 belongs to the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (UGAUGA) and the D box (CUGA). Most of the members of the box C/D family function in directing site-specific 2'-O-methylation of substrate RNAs. snoRNA snR71 was initially discovered using a computational screen of the Saccharomyces cerevisiae genome. | Small nucleolar RNA snR71 |
c_cw5df120d21j | In molecular biology, subcloning is a technique used to move a particular DNA sequence from a parent vector to a destination vector. Subcloning is not to be confused with molecular cloning, a related technique. | Subcloning |
c_kwhqruz7vcro | In molecular biology, tRNA-dihydrouridine synthase is a family of enzymes which catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. | TRNA-dihydrouridine synthase |
c_o4nhd5vsaz5h | It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae (Baker's yeast) acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. | TRNA-dihydrouridine synthase |
c_2tjgzwanx1vn | Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria. == References == | TRNA-dihydrouridine synthase |
c_t5phy57lq7ch | In molecular biology, the (ADP-ribosyl)hydrolase (ARH) family contains enzymes which catalyses the hydrolysis of ADP-ribosyl modifications from proteins, nucleic acids and small molecules. | ADP-ribosylhydrolase |
c_6hswdof1uplq | In molecular biology, the 3H domain is a protein domain named after its three highly conserved histidine residues. The 3H domain appears to be a smarr molecure-binding domain, based on its occurrence with other domains. Several proteins carrying this domain are transcriptional regulators from the biotin repressor family. The transcription regulator TM1602 from Thermotoga maritima is a DNA-binding protein thought to belong to a family of de novo NAD synthesis pathway regulators. | 3H domain |
c_e32tzuvk0ssz | TM1602 has an N-terminal DNA-binding domain and a C-terminal 3H regulatory domain. The N-terminal domain appears to bind to the NAD promoter region and repress the de novo NAD biosynthesis operon, while the C-terminal 3H domain may bind to nicotinamide, nicotinic acid, or other substrate/products. The 3H domain has a 2-layer alpha/beta sandwich fold. == References == | 3H domain |
c_lvgfs2pqgirh | In molecular biology, the 5.8S ribosomal RNA (5.8S rRNA) is a non-coding RNA component of the large subunit of the eukaryotic ribosome and so plays an important role in protein translation. It is transcribed by RNA polymerase I as part of the 45S precursor that also contains 18S and 28S rRNA. Its function is thought to be in ribosome translocation. It is also known to form covalent linkage to the p53 tumour suppressor protein. | 5.8S rRNA |
c_h7azsepkkw0c | 5.8S rRNA can be used as a reference gene for miRNA detection. The 5.8S ribosomal RNA is used to better understand other rRNA processes and pathways in the cell.The 5.8S rRNA is homologous to the 5' end of non-eukaryotic LSU rRNA. In eukaryotes, the insertion of ITS2 breaks LSU rRNA into 5.8S and 28S rRNAs. Some flies have their 5.8 rRNA further split into two pieces. | 5.8S rRNA |
c_aq0hd5gnkoez | In molecular biology, the ABM domain is a protein domain that is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species, which can carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The structure of ActVA-Orf6 monooxygenase from Streptomyces coelicolor, which is involved in actinorhodin biosynthesis, reveals a dimeric alpha+beta barrel topology. There is also a conserved histidine that is likely to be an active site residue. In the S. coelicolor protein SCO1909 this domain occurs as a repeat. == References == | ABM domain |
c_i4ve9likrkdv | In molecular biology, the ACT domain is a protein domain that is found in a variety of proteins involved in metabolism. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. The ACT domain is named after three of the proteins that contain it: aspartate kinase, chorismate mutase and TyrA. The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. | ACT domain |
c_f9ld2b8o548k | A pair of ACT domains form an eight-stranded antiparallel sheet with two molecules of allosteric inhibitor serine bound in the interface. Biochemical exploration of a few other proteins containing ACT domains supports the suggestions that these domains contain the archetypical ACT structure.The ACT domain was discovered by Aravind and Koonin using iterative sequence searches. == References == | ACT domain |
c_xcu1xtycil1c | In molecular biology, the AMMECR1 protein (Alport syndrome, intellectual disability, midface hypoplasia and elliptocytosis chromosomal region gene 1 protein) is a protein encoded by the AMMECR1 gene on human chromosome Xq22.3. The contiguous gene deletion syndrome is characterised by Alport syndrome (A), intellectual disability (M), midface hypoplasia (M), and elliptocytosis (E), as well as generalized hypoplasia and cardiac abnormalities. It is caused by a deletion in Xq22.3, comprising several genes including AMME chromosomal region gene 1 (AMMECR1), which encodes a protein with a nuclear location and presently unknown function. | AMMECR1 |
c_zi9ga0btx2ua | The C-terminal region of AMMECR1 (from residue 122 to 333) is well conserved, and homologues appear in species ranging from bacteria and archaea to eukaryotes. The high level of conservation of the AMMECR1 domain points to a basic cellular function, potentially in either the transcription, replication, repair or translation machinery.The AMMECR1 domain contains a six-amino-acid motif (LRGCIG) that might be functionally important since it is strikingly conserved throughout evolution. The AMMECR1 domain consists of two distinct subdomains of different sizes. | AMMECR1 |
c_67vozqiyowec | The large subdomain, which contains both the N- and C-terminal regions, consists of five alpha-helices and five beta-strands. These five beta-strands form an antiparallel beta-sheet. The small subdomain consists of four alpha-helices and three beta-strands, and these beta-strands also form an antiparallel beta-sheet. | AMMECR1 |
c_03rmzgtbd0cx | The conserved 'LRGCIG' motif is located at beta(2) and its N-terminal loop, and most of the side chains of these residues point toward the interface of the two subdomains. The two subdomains are connected by only two loops, and the interaction between the two subdomains is not strong. Thus, these subdomains may move dynamically when the substrate enters the cleft. | AMMECR1 |
c_y10d77qt18no | The size of the cleft suggests that the substrate is large, e.g., the substrate may be a nucleic acid or protein. However, the inner side of the cleft is not filled with positively charged residues, and therefore it is unlikely that negatively charged nucleic acids such as DNA or RNA interact at this site. == References == | AMMECR1 |
c_f6p3lz1fwusg | In molecular biology, the AN1-type zinc finger domain, which has a dimetal (zinc)-bound alpha/beta fold. This domain was first identified as a zinc finger at the C terminus of AN1 SWISSPROT, a ubiquitin-like protein in Xenopus laevis. The AN1-type zinc finger contains six conserved cysteines and two histidines that could potentially coordinate 2 zinc atoms. Certain stress-associated proteins (SAP) contain AN1 domain, often in combination with A20 zinc finger domains (SAP8) or C2H2 domains (SAP16). | AN1 zinc finger |
c_da03iftq1jgf | For example, the human protein Znf216 has an A20 zinc-finger at the N terminus and an AN1 zinc-finger at the C terminus, acting to negatively regulate the NFkappaB activation pathway and to interact with components of the immune response like RIP, IKKgamma and TRAF6. The interact of Znf216 with IKK-gamma and RIP is mediated by the A20 zinc-finger domain, while its interaction with TRAF6 is mediated by the AN1 zinc-finger domain; therefore, both zinc-finger domains are involved in regulating the immune response. The AN1 zinc finger domain is also found in proteins containing a ubiquitin-like domain, which are involved in the ubiquitination pathway. | AN1 zinc finger |
c_m749fxrtaz6b | Proteins containing an AN1-type zinc finger include: Ascidian posterior end mark 6 (pem-6) protein . Human AWP1 protein (associated with PRK1), which is expressed during early embryogenesis. Human immunoglobulin mu binding protein 2 (SMUBP-2), mutations in which cause muscular atrophy with respiratory distress type 1.AN1-type zinc finger domains are widely present across diverse "Euryarchaeota" and Nitrososphaerota, where they are often fused to membrane-associated peptidase domains such as the rhomboid family serine peptidase, transglutaminase-like thiol peptidases of the papain fold, and Zn-dependent metallopeptidases. | AN1 zinc finger |
c_mwr6atuuisll | Archaeal AN1 domains are also linked to transmembrane helices, and domains such as DNAJ and SCP/PR1. These fusions suggest membrane-associated roles for AN1 domain containing proteins in archaea, such as in proteolytic processing of polypeptides and in regulating protein folding or stability. The architectural syntax is remarkably similar to that of the prokaryotic B-box zinc finger and LIM domains. == References == | AN1 zinc finger |
c_b19hfn7aeufs | In molecular biology, the ARID domain (AT-rich interaction domain; also known as BRIGHT (B-cell Regulator of Ig Heavy chain Transcription) domain)) is a protein domain that binds to DNA. ARID domain-containing proteins are found in fungi, plants and invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative transcriptional regulation and a likely involvement in the modification of chromatin structure. | ARID domain |
c_i21imwv36s5i | The basic structure of the ARID domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence homology, they can be partitioned into three structural classes: Minimal ARID proteins that consist of a core domain formed by six alpha helices; ARID proteins that supplement the core domain with an N-terminal alpha-helix; and Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini. The human SWI-SNF complex protein ARID1A is an ARID family member with non-sequence-specific DNA binding activity. | ARID domain |
c_0flnlbrbn1e6 | The ARID consensus and other structural features are common to both ARID1A and yeast SWI1, suggesting that ARID1A is a human counterpart of SWI1. The approximately 100-residue ARID sequence is present in a series of proteins strongly implicated in the regulation of cell growth, development, and tissue-specific gene expression. Although about a dozen ARID proteins can be identified from database searches, to date, only Bright (a regulator of B-cell-specific gene expression), dead ringer (a Drosophila melanogaster gene product required for normal development), and MRF-2 (which represses expression from the Cytomegalovirus enhancer) have been analyzed directly with regard to their DNA binding properties. | ARID domain |
c_huoxohgw8aoj | Each binds preferentially to AT-rich sites. In contrast, ARID1A shows no sequence preference in its DNA binding activity, thereby demonstrating that AT-rich binding is not an intrinsic property of ARID domains and that ARID family proteins may be involved in a wider range of DNA interactions. == References == | ARID domain |
c_1kk7xmr943wd | In molecular biology, the ASF1 like histone chaperone family of proteins includes the yeast and human ASF1 proteins. These proteins are of the chaperone protein group and in particular can be placed into the histone chaperone subgroup. ASF1 participates in both the replication-dependent and replication-independent pathways. The three-dimensional structure has been determined as a compact immunoglobulin-like beta sandwich fold topped by three helical linkers. == References == | ASF1 like histone chaperone |
c_k83gfme9ahzd | In molecular biology, the ATCase/OTCase family is a protein family which contains two related enzymes: aspartate carbamoyltransferase EC 2.1.3.2 and ornithine carbamoyltransferase EC 2.1.3.3. It has been shown that these enzymes are evolutionary related. The predicted secondary structure of both enzymes is similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies to be implicated in binding the phosphoryl group of carbamoyl phosphate and may also play a role in trimerisation of the molecules. | ATCase/OTCase family |
c_53lnjd6lzb1p | The N-terminal domain is the carbamoyl phosphate binding domain. The C-terminal domain is an aspartate/ornithine-binding domain. Aspartate carbamoyltransferase (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides. | ATCase/OTCase family |
c_bers2tggml9e | In prokaryotes ATCase consists of two subunits: a catalytic chain (gene pyrB) and a regulatory chain (gene pyrI), while in eukaryotes it is a domain in a multi- functional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals) that also catalyzes other steps of the biosynthesis of pyrimidines.Ornithine carbamoyltransferase (OTCase) catalyses the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals this enzyme participates in the urea cycle and is located in the mitochondrial matrix. In prokaryotes and eukaryotic microorganisms it is involved in the biosynthesis of arginine. In some bacterial species it is also involved in the degradation of arginine (the arginine deaminase pathway). == References == | ATCase/OTCase family |
c_3pegmwu2bkco | In molecular biology, the ATP-cone is an evolutionarily mobile, ATP-binding regulatory domain which is found in a variety of proteins including ribonucleotide reductases, phosphoglycerate kinases and transcriptional regulators.In ribonucleotide reductase protein R1 from Escherichia coli this domain is located at the N terminus, and is composed mostly of helices. It forms part of the allosteric effector region and contains the general allosteric activity site in a cleft located at the tip of the N-terminal region. This site binds either ATP (activating) or dATP (inhibitory), with the base bound in a hydrophobic pocket and the phosphates bound to basic residues. Substrate binding to this site is thought to affect enzyme activity by altering the relative positions of the two subunits of ribonucleotide reductase. == References == | ATP cone |
c_337aycqodwbq | In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes, that reversibly catalyse the transfer of phosphate between ATP and various phosphagens. The enzymes belonging to this family include: Glycocyamine kinase (EC 2.7.3.1), which catalyses the transfer of phosphate from ATP to guanidoacetate. Arginine kinase (EC 2.7.3.3), which catalyses the transfer of phosphate from ATP to arginine. Taurocyamine kinase (EC 2.7.3.4), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to taurocyamine. | ATP:guanido phosphotransferase family |
c_c11akf4uksgp | Lombricine kinase (EC 2.7.3.5), an annelid-specific enzyme that catalyses the transfer of phosphate from ATP to lombricine. Smc74, a cercaria-specific enzyme from Schistosoma mansoni. Creatine kinase (EC 2.7.3.2) (CK), which catalyses the reversible transfer of high energy phosphate from ATP to creatine, generating phosphocreatine and ADP.Creatine kinase plays an important role in energy metabolism of vertebrates. | ATP:guanido phosphotransferase family |
c_99bwylxrb8wb | There are at least four different, but very closely related, forms of CK. Two isozymes, M (muscle) and B (brain), are cytosolic, while the other two are mitochondrial. In sea urchins there is a flagellar isozyme, which consists of the triplication of a CK-domain. | ATP:guanido phosphotransferase family |
c_g0m7k39t2r02 | A cysteine residue is implicated in the catalytic activity of these enzymes and the region around this active site residue is highly conserved. ATP:guanido phosphotransferases contain a C-terminal catalytic domain which consists of a duplication where the common core consists of two beta-alpha-beta2-alpha repeats. The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. They also contain an N-terminal domain which has an all-alpha fold consisting of an irregular array of 6 short helices. == References == | ATP:guanido phosphotransferase family |
c_z0ioeg1wf4c1 | In molecular biology, the Acyl-CoA-binding protein (ACBP) is a small (10 Kd) protein that binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. ACBP is also known as diazepam binding inhibitor (DBI) or endozepine (EP) because of its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.ACBP is a highly conserved protein of about 90 amino acids that is found in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and in some eubacterial species.Although ACBP occurs as a completely independent protein, intact ACB domains have been identified in a number of large, multifunctional proteins in a variety of eukaryotic species. These include large membrane-associated proteins with N-terminal ACB domains, multifunctional enzymes with both ACB and peroxisomal enoyl-CoA Delta(3), Delta(2)-enoyl-CoA isomerase domains, and proteins with both an ACB domain and ankyrin repeats.The ACB domain consists of four alpha-helices arranged in a bowl shape with a highly exposed acyl-CoA-binding site. | Acyl-CoA-binding protein |
c_6vujihga7z23 | The ligand is bound through specific interactions with residues on the protein, most notably several conserved positive charges that interact with the phosphate group on the adenosine-3'phosphate moiety, and the acyl chain is sandwiched between the hydrophobic surfaces of CoA and the protein.Other proteins containing an ACB domain include: Endozepine-like peptide (ELP) (gene DBIL5) from mouse. ELP is a testis-specific ACBP homologue that may be involved in the energy metabolism of the mature sperm. MA-DBI, a transmembrane protein of unknown function which has been found in mammals. | Acyl-CoA-binding protein |
c_1flbudp0do9g | MA-DBI contains a N-terminal ACB domain. DRS-1, a human protein of unknown function that contains a N-terminal ACB domain and a C-terminal enoyl-CoA isomerase/hydratase domain. == References == | Acyl-CoA-binding protein |
c_5e6fsy6ruxlm | In molecular biology, the BAH domain (bromo-adjacent homology) domain is found in proteins such as eukaryotic DNA (cytosine-5) methyltransferases, the origin recognition complex 1 (Orc1) proteins, Bromo adjacent homology domain containing 1 (BAHD1), as well as several proteins involved in transcriptional regulation. The BAH domain appears to act as a protein-protein interaction module specialised in gene silencing, as suggested for example by its interaction within yeast Orc1p with the silent information regulator Sir1p. The BAH domain might therefore play an important role by linking DNA methylation, replication and transcriptional regulation. == References == | BAH domain |
c_1kcetm8zrdak | In molecular biology, the BEN domain is a protein domain which is found in diverse proteins including: SMAR1 (Scaffold/Matrix attachment region-binding protein 1; also known as BANP), a tumour-suppressor MAR-binding protein that down-regulates Cyclin D1 expression by recruiting HDAC1-mSin3A co-repressor complex at Cyclin D1 promoter locus; SMAR1 is the target of prostaglandin A2 (PGA2) induced growth arrest. NACC1, a novel member of the POZ/BTB (Pox virus and Zinc finger/Broad complex, Tramtrack and Bric-a-brac), but which varies from other proteins of this class in that it lacks the characteristic DNA-binding motif. Mod(mdg4) isoform C, the modifier of the mdg4 locus in Drosophila melanogaster (Fruit fly), where mdg4 encodes chromatin proteins which are involved in position effect variegation, establishment of chromatin boundaries, nerve path finding, meiotic chromosome pairing and apoptosis. | BEN domain |
c_mcbebozat90c | Trans-splicing of Mod(mdg4) produces at least 26 transcripts. BEND2, a protein of unknown function, that is predicted to be involved in chromatin modification and has been associated clinically with central nervous system disorders. E5R protein from Chordopoxvirus virosomes, which is found in cytoplasmic sites of viral DNA replication. | BEN domain |
c_wfjvrf4mi90i | Several proteins of polydnaviruses.The BEN domain is predicted to function as an adaptor for the higher-order structuring of chromatin, and recruitment of chromatin modifying factors in transcriptional regulation. It has been suggested to mediate protein-DNA and protein-protein interactions during chromatin organization and transcription. The presence of BEN domains in a poxviral early virosomal protein and in polydnaviral proteins also suggests a possible role in the organisation of viral DNA during replication or transcription. | BEN domain |
c_17ujx46evce8 | They are generally linked to other globular domains with functions related to transcriptional regulation and chromatin structure, such as BTB, C4DM, and C2H2 fingers.This domain is predicted to form an all-alpha fold with four conserved helices. Its conservation pattern revealed several conserved residues, most of which have hydrophobic side-chains and are likely to stabilize the fold through helix-helix packing. First human BEN domain (BEND3)structure is solved together with TPR (ERCC6L)domain and Stimulates the ERCC6L translocase and ATPase activities. | BEN domain |
c_qof8msosvewv | In molecular biology, the BESS domain is a protein domain which has been named after the three proteins that originally defined the domain: BEAF (Boundary element associated factor 32), Suvar(3)7 and Stonewall ). The BESS domain is 40 amino acid residues long and is predicted to be composed of three alpha helices, as such it might be related to the myb/SANT HTH domain. The BESS domain directs a variety of protein-protein interactions, including interactions with itself, with Dorsal, and with a TBP-associated factor. It is found in a single copy in Drosophila proteins and is often associated with the MADF domain.Proteins known to contain a BESS domain include: Drosophila Boundary element associated factor 32 (BEAF-32). | BESS domain |
c_09oqbalez9ra | Drosophila Suppressor of variegation protein 3-7 (Su(var)3-7), which could play a role in chromosome condensation. Drosophila Ravus, which is homologous to the C-terminal part of Su(var)3-7. Drosophila Stonewall (Stwl), a putative transcription factor required for maintenance of female germline stem cells as well as oocyte differentiation. | BESS domain |
c_0ixoinu4dp7l | Drosophila Adf-1, a transcription factor first identified on the basis of its interaction with the alcohol dehydrogenase promoter but that binds the promoters of a diverse group of genes. Drosophila Dorsal-interacting protein 3 (Dip3). It functions both as an activator to bind DNA in a sequence specific manner and a coactivator to stimulate synergistic activation by Dorsal and Twist. == References == | BESS domain |
c_3j2cq0fe2hos | In molecular biology, the BLUF domain (sensors of blue-light using FAD) is a FAD-binding protein domain. They are present in various proteins, primarily from bacteria, for example a BLUF domain is found at the N-terminus of the AppA protein from Rhodobacter sphaeroides. The BLUF domain is involved in sensing blue-light (and possibly redox) using FAD and is similar to the flavin-binding PAS domains and cryptochromes. The predicted secondary structure reveals that the BLUF domain has a novel FAD-binding fold. == References == | BLUF domain |
c_kwqencqx1c4d | In molecular biology, the BPS domain (Between PH and SH2) domain is a protein domain of approximately 45 amino acids found in the adaptor proteins Grb7/|Grb10/Grb14. It mediates inhibition of the tyrosine kinase domain of the insulin receptor by binding of the N-terminal portion of the BPS domain to the substrate peptide groove of the kinase, acting as a pseudosubstrate inhibitor. It is composed of two beta strands and a C-terminal helix. == References == | BPS domain |
c_0mozsenlxb51 | In molecular biology, the BSD domain is an approximately 60-amino-acid-long protein domain named after the BTF2-like transcription factors, synapse-associated proteins and DOS2-like proteins in which it is found. It is also found in several hypothetical proteins. It occurs in one or two copies in a variety of species ranging from primal protozoan to human, and can be found associated with other domains such as the BTB domain or the U-box in multidomain proteins. Its function is as yet unknown.Secondary structure prediction indicates the presence of three predicted alpha helices, which probably form a three-helical bundle in small |domains. | BSD domain |
c_3eod4cbmnr5b | The third predicted helix contains neighbouring phenylalanine and tryptophan residues—less common amino acids that are invariant in all the BSD domains identified and that are the domain's most striking sequence features.Some proteins known to contain one or two BSD domains are: Mammalian TFIIH basal transcription factor complex p62 subunit (GTF2H1). Yeast RNA polymerase II transcription factor B 73 kDa subunit (TFB1), the homologue of BTF2. Yeast DOS2 protein, involved in single-copy DNA replication and ubiquitination. | BSD domain |
c_mnen621g7lsg | Drosophila synapse-associated protein SAP47. Mammalian SYAP1. Various Arabidopsis thaliana (mouse-ear cress) hypothetical proteins. | BSD domain |
c_zs4xkxaguvum | In molecular biology, the BURP domain is a ~230-amino acid protein domain, which has been named for the four members of the group initially identified, BNM2, USP, RD22, and PG1beta. It is found in the C-terminal part of a number of plant cell wall proteins, which are defined not only by the BURP domain, but also by the overall similarity in their modular construction. The BURP domain proteins consists of either three or four modules: (i) an N-terminal hydrophobic domain - a presumptive transit peptide, joined to (ii) a short conserved segment or other short segment, (iii) an optional segment consisting of repeated units which is unique to each member, and (iv) the C-terminal BURP domain. Although the BURP domain proteins share primary structural features, their expression patterns and the conditions under which they are expressed differ. | BURP domain |
c_4esylsjhe047 | The presence of the conserved BURP domain in diverse plant proteins suggests an important role for this domain. It is possible that the BURP domain represents a general motif for localization of proteins within the cell wall matrix. The other structural domains associated with the BURP domain may specify other target sites for intermolecular interactions.Some proteins known to contain a BURP domain are listed below: Brassica protein BNM2, which is expressed during the induction of microspore embryogenesis. | BURP domain |
c_ur6wyl37gb0e | Field bean USPs, abundant non-storage seed proteins with unknown function. Soybean USP-like proteins ADR6 (or SALI5-4A), an auxin-repressible, aluminium-inducible protein and SALI3-2, a protein that is up-regulated by aluminium. Soybean seed coat BURP-domain protein 1 (SCB1). | BURP domain |
c_y8wuheoouchl | It might play a role in the differentiation of the seed coat parenchyma cells. Arabidopsis RD22 drought induced protein. Maize ZRP2, a protein of unknown function in cortex parenchyma. | BURP domain |
c_nzdqekjkfi4x | Tomato PG1beta, the beta-subunit of polygalacturonase isozyme 1 (PG1), which is expressed in ripening fruits. Cereal RAFTIN. It is essential specifically for the maturation phase of pollen development. == References == | BURP domain |
c_lw2dprua2gbh | In molecular biology, the Bacillus haemolytic enterotoxin family of proteins consists of several Bacillus haemolytic enterotoxins (HblC, HblD, HblA, NheA, and NheB), which can cause food poisoning in humans. Haemolysin BL (encoded by HBL) and non-haemolytic enterotoxin (encoded by NHE), represent the major enterotoxins produced by Bacillus cereus. Most of the cytotoxic activity of B. cereus isolates has been attributed to the level of Nhe, which may indicate a highly diarrheic potential. The exact mechanism by which B. cereus causes diarrhoea is unknown. | Bacillus haemolytic enterotoxin |
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